Preorganized secondary structure as an important determinant of fast protein folding

199 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

RaptorX-Property: a web server for protein structure property prediction (2016, background): “Job name (1) and user email address (2) are optional.”
Protein 8-class secondary structure prediction using conditional neural fields (2010, background): “It will help in protein tertiary structure prediction and functional annotation if the SS is known [4].”
Knowledge-based machine learning methods for macromolecular 3D structure prediction (2016, background): “Thus, it is used by biologists to identify protein function (Myers and Oas, 2001).”
The protein folding problem. (2008, background): “Some proteins, such as helical bundles, appear to follow a hierarchical diffusion-collision model (155, 169) in which secondary structure forms and assembles in a hierarchical order.”
The protein folding 'speed limit'. (2004, unknown): “3 310 [127] [91,119,128–146]”
Is there a unifying mechanism for protein folding? (2003, background): “Proteins listed are discussed in the text aside from: protein A [ 48 ], tenascin [49], FKBP12 [50] and lysozyme [51].”
Affibody molecules: Engineered proteins for therapeutic, diagnostic and biotechnological applications (2010, background): “The B-domain is a relatively short cysteine-free peptide of 58 amino acids that is folded into a three-helical bundle structure and the kinetics of the folding reaction is one of the fastest that has been reported [4].”